Evidence map›Paper›PMID 27297677›Full record

ArticlePlant physiology2016

Lack of FTSH4 Protease Affects Protein Carbonylation, Mitochondrial Morphology, and Phospholipid Content in Mitochondria of Arabidopsis: New Insights into a Complex Interplay.

Elwira Smakowska, Renata Skibior-Blaszczyk, Malgorzata Czarna, Marta Kolodziejczak, Malgorzata Kwasniak-Owczarek, Katarzyna Parys, Christiane Funk, Hanna Janska

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Plants (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Plant Mitophagy in Comparison to Mammals: What Is Still Missing?International journal of molecular sciences · 2021
    Review
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 2 countries.

Elwira SmakowskaFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Renata Skibior-BlaszczykFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Malgorzata CzarnaFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Marta KolodziejczakFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Malgorzata Kwasniak-OwczarekFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Katarzyna ParysFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.).
Christiane FunkFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.) christiane.funk@umu.se janska@ibmb.uni.wroc.pl.ORCID 0000-0002-7897-4038
Hanna JanskaFaculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland (E.S., R.S.-B, M.C., M.K., M.K.-O., K.P., H.J.); andDepartment of Chemistry, Umeå University, 901 87 Umea, Sweden (C.F.) christiane.funk@umu.se janska@ibmb.uni.wroc.pl.ORCID 0000-0002-6542-343X
University of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FTSH4 is one of the inner membrane-embedded ATP-dependent metalloproteases in mitochondria of Arabidopsis (Arabidopsis thaliana). In mutants impaired to express FTSH4, carbonylated proteins accumulated and leaf morphology was altered when grown under a short-day photoperiod, at 22°C, and a long-day photoperiod, at 30°C. To provide better insight into the function of FTSH4, we compared the mitochondrial proteomes and oxyproteomes of two ftsh4 mutants and wild-type plants grown under conditions inducing the phenotypic alterations. Numerous proteins from various submitochondrial compartments were observed to be carbonylated in the ftsh4 mutants, indicating a widespread oxidative stress. One of the reasons for the accumulation of carbonylated proteins in ftsh4 was the limited ATP-dependent proteolytic capacity of ftsh4 mitochondria, arising from insufficient ATP amount, probably as a result of an impaired oxidative phosphorylation (OXPHOS), especially complex V. In ftsh4, we further observed giant, spherical mitochondria coexisting among normal ones. Both effects, the increased number of abnormal mitochondria and the decreased stability/activity of the OXPHOS complexes, were probably caused by the lower amount of the mitochondrial membrane phospholipid cardiolipin. We postulate that the reduced cardiolipin content in ftsh4 mitochondria leads to perturbations within the OXPHOS complexes, generating more reactive oxygen species and less ATP, and to the deregulation of mitochondrial dynamics, causing in consequence the accumulation of oxidative damage.

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsCarrier ProteinsMembrane ProteinsMetalloproteasesMitochondriaMitochondrial MembranesMitochondrial Proton-Translocating ATPasesOxidation-ReductionOxidative PhosphorylationOxidative StressPlant LeavesProtein CarbonylationReactive Oxygen SpeciesAdenosine TriphosphatasesArabidopsis ProteinsCarrier ProteinsFtsH4 protein, ArabidopsisMembrane ProteinsMetalloproteasesMitochondrial Proton-Translocating ATPasesoligomycin sensitivity-conferring proteinReactive Oxygen Species

Identifiers

PMID27297677
PMCPMC4972270
OpenAlexW2426497164

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.